A motion tracking method that applies a spread spectrum communication technique to tagging MR imaging.

PURPOSE: We propose a new motion tracking method that encodes an object's position information using tagging magnetic resonance (MR) images as digital codes, and we assess the method's feasibility in stationary and moving phantoms. The encoding and decoding of tag patterns employ principles of spread spectrum communication. METHODS: We used a segmented fast low angle shot cine sequence (FLASH) with spatial modulation of magnetization (SPAMM) preparation pulses to encode position information as 7-bit code words and used this spread code to decode the position information. To make 7-bit code words using tag images, we adjusted the flip angle and phase of the 4 composite radiofrequency (RF) pulses and the gradient magnetic field strength in the SPAMM pulse to generate 7 types of tag patterns. The proposed method required 7 acquisitions with 7 types of tag patterns. We compared results with images obtained by conventional tagging in stationary and moving phantom experiments. RESULTS: In a stationary phantom, the proposed method showed the same ability to identify pixel position as conventional tagging method using improved SNR images with the average of 7 acquisitions. In a moving phantom, pixel position was successfully decoded by the proposed method on a pixel-by-pixel basis. In this method, the motion of the phantom was detected by the simple calculation of the correlation coefficient of the code words. CONCLUSION: We introduced a spread spectrum communication technique to tagging MR imaging that regards tag patterns as digital codes, and we demonstrated the method's potential to detect pixel position in sub-pixel resolution.

Preparation and O2 binding study of myoglobin having a cobalt porphycene.

Sperm whale myoglobin, an oxygen-storage hemoprotein, was reconstituted with 2,7-diethyl-3,6,12,17-tetramethyl-13,16-bis(carboxyethyl)porphycenatocobalt(II) in order to investigate the reactivities of a cobalt porphycene in a protein matrix. Similar to the previously reported finding for the myoglobin with the iron porphycene, the reconstituted myoglobin with the cobalt porphycene was also found to have an O2 affinity 2 orders of magnitude greater than that of the myoglobin possessing cobalt protoporphyrin IX. The EPR spectra of the deoxy and oxy myoglobins having the cobalt porphycene at 77 K also have features similar to those of the myoglobin with cobalt protoporphyrin IX. These spectra suggest that the porphycene cobalt in the deoxy form is coordinated by one nitrogenous ligand postulated to be the imidazole ring of His93, and that the bond configuration of CoII-O2 is regarded as the CoIII-Omicron2*- species.